Research workbench
1.15 ångström crystal structure of the MA3 domain of PDCD4
Analyse 1.15 ångström crystal structure of the MA3 domain of PDCD4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NSZ
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Programmed cell death protein 4
- UniProt
- Q61823
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Programmed cell death protein 4 | protein | 129 | 77% helix, 0% strand | Q61823 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2NSZ · 1.15 Angstrom Crystal Structure of the MA3 domain of Pdcd4 · the same entry in another collection · chain A against A, TM-score 1.00
- Q61823 · AlphaFold monomer V2.0 prediction for programmed cell death protein 4 (Q61823) · a predicted model of the same protein · chain A against A, TM-score 0.96
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q61823
- Elsewhere: RCSB PDB 2NSZ · PDBe 2NSZ · UniProt Q61823
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